MAGNETIC-FIELD EFFECTS ON B-12 ETHANOLAMINE AMMONIA-LYASE - EVIDENCE FOR A RADICAL MECHANISM
MAGNETIC-FIELD EFFECTS ON B-12 ETHANOLAMINE AMMONIA-LYASE - EVIDENCE FOR A RADICAL MECHANISM
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DOI：
10.1126/science.8310292
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发表时间：
1994-02-18
期刊：
影响因子：
56.9
通讯作者：
GRISSOM, CB
中科院分区：
文献类型：
--
作者：
HARKINS, TT;GRISSOM, CB
自由基对重组率的变化是磁场与生物系统相互作用的为数不多的机制之一。依赖辅酶B-12的乙醇胺解氨酶的动力学参数V-max/K-m(其中K-m为米氏常数)在0.1Tesla(1000Gauss)附近的恒磁场下降低了25%，而在0.15Tesla附近的恒磁场下，过氢乙醇胺的动力学参数降低了60%。这一效应可能是由于磁场引起的自旋相关自由基对中的单态和三态自旋态之间的交叉率发生了变化。
A change in radical pair recombination rates is one of the few mechanisms by which a magnetic field can interact with a biological system. The kinetic parameter V-max/K-m (where K-m is the Michaelis constant) for the coenzyme B-12-dependent enzyme ethanolamine ammonia lyase was decreased 25 percent by a static magnetic field near 0.1 tesla (1000 gauss) with unlabeled ethanolamine and decreased 60 percent near 0.15 tesla with perdeuterated ethanolamine. This effect is likely caused by a magnetic field-induced change in intersystem crossing rates between the singlet and triplet spin states in the {cob(II)alamin:5'-deoxyadenosyl radical} spin-correlated radical pair.